Alignment Of Strands Research Articles

Casting Blood Circulations

In this article I examine three Bengali translations of texts about blood circulation from the last decade and a half of the nineteenth century. Through a close examination of these three translations, I demonstrate the importance of what Antonio Gramsci called “translatability” and what I have elsewhere called “braided sciences.” Taken together, these two heuristic devices demonstrate a relationship between social hierarchies and translation, on the one hand, and a selective alignment of various strands of epistemic, technological, and narrative traditions on the other. One of the principal objectives of the article is to recenter the importance of caste and social hierarchy in understanding colonial knowledge production.

Micro-homology intermediates: RecA's transient sampling revealed at the single molecule level.

Recombinase A (RecA) is central to homologous recombination. However, despite significant advances, the mechanism with which RecA is able to orchestrate a search for homology remains elusive. DNA nanostructure-augmented high-speed AFM offers the spatial and temporal resolutions required to study the RecA recombination mechanism directly and at the single molecule level. We present the direct in situ observation of RecA-orchestrated alignment of homologous DNA strands to form a stable recombination product within a supporting DNA nanostructure. We show the existence of subtle and short-lived states in the interaction landscape, which suggests that RecA transiently samples micro-homology at the single RecA monomer-level throughout the search for sequence alignment. These transient interactions form the early steps in the search for sequence homology, prior to the formation of stable pairings at >8 nucleotide seeds. The removal of sequence micro-homology results in the loss of the associated transient sampling at that location.

From the President and IFST News

From the President and IFST News

Molecular anisotropy and rearrangement as mechanisms of toughness and extensibility in entangled physical gels

Dynamic networks formed by physically crosslinked, entangled polymers have emerged as self-healing, stretchable, and functional materials. Entangled associative gels with remarkable toughness and extensibility have been produced by several distinct chemical approaches, suggesting that these enhanced mechanical properties result from molecular-scale topology. Previously, artificially engineered associative proteins were designed to provide an ideal model system to investigate the role of entanglement on gel mechanics via well-defined entangled or unentangled physical gels. Herein, uniaxial strain-induced structural changes in these model gels were observed using in situ small-angle x-ray scattering (SAXS) and in situ polarized optical microscopy (POM) up to 2000% engineering strain. Anisotropic optical responses to uniaxial strain at the nano-, micro-, and macroscales suggest that stress dissipation mechanisms enable high extensibility and toughness. Nano- and microscopic anisotropy observed by SAXS indicate stretching and alignment of flexible polymer strands along the straining axis, and nonmonotonic macroscopic anisotropy observed by POM suggests relaxation within the hydrogel due to rearrangement of associative network junctions. Unentangled hydrogels exhibit low toughness and a strain-rate-dependent transition from ductile to brittle tensile behavior, which is typical for associative polymer solutions. These findings indicate that topological entanglements and the freedom of individual chains to align at the nanoscale due to junction relaxation are both critical to achieving high toughness and elongation in entangled physical gels.

Pre-stability and functional tests of a leave-on hair emulsion developed with Aloe vera extract

Leave-on creams are cationic emulsions with lower active content than conditioners. They are a complement to the comb and contain agents that moisturize hair and return to it the effect of conditioners, facilitating hairstyle. The part of the plant which is used is the mucilage obtained from the leaves, as it has emollient and moisturizing properties. The purpose of this paper was to develop a leave-on emulsion containing Aloe vera extract, obtained by two different extraction methods, and one extract acquired commercially in order to evaluate its pre-stability and functionality in hair strands. The formulation of the leave-on emulsion was developed with Aloe vera extracts. These extracts were prepared with plant material (PM) plus 70% alcohol (Sample A) and PM, cereal alcohol and glycerin (Sample B). The pre-stability test was performed according to ANVISA Guide. We analysed tests on human hair strands to assess combability (after shampooing them with neutral shampoo, the standardized amount of the sample was spread on strands, which were combed to observe the slip point after 10 combing strokes) and appearance after drying (the strands were left hanging at 23°C and 33% humidity for 24 hours) and softness to the touch and volume (photographed data). In the pre-stability test, the samples were stable in color, odor, appearance and centrifugation test under all conditions, except in samples that were exposed to direct sunlight, when they were modified in color and odor. The pH remained stable in all samples and under all conditions. The spreadability went through which were not relevant to the formulation tested. For the tests on strands of hair, one of the samples was the base formulation without adding the plant extract, for comparison purposes. The average results of the strands test of all samples were 9.87 cm ± 0.6875 of sliding length, which were much greater when compared to the untreated sample that slid only 5 cm. After drying, the strands looked softer. There was softness to the touch, volume reduction and alignment of the hair strands, when compared to the untreated strands. We concluded that the base emulsion formulation, by its own, showed improvement in the hair strands for combing and appearance after drying. The formulations containing the extract showed no improvement in the tests on strands, when compared with the base formulation. The formulations developed have favorable results in the physicochemical pre-stability tests.

Amyloid Beta Peptide Folding in Reverse Micelles.

Previously published experimental studies have suggested that when the 40-residue amyloid beta peptide is encapsulated in a reverse micelle, it folds into a structure that may nucleate amyloid fibril formation (Yeung, P. S.-W.; Axelsen, P. H. J. Am. Chem. Soc. 2012, 134, 6061 ). The factors that induce the formation of this structure have now been identified in a multi-microsecond simulation of the same reverse micelle system that was studied experimentally. Key features of the polypeptide-micelle interaction include the anchoring of a hydrophobic residue cluster into gaps in the reverse micelle surface, the formation of a beta turn at the anchor point that brings N- and C-terminal segments of the polypeptide into proximity, high ionic strength that promotes intramolecular hydrogen bond formation, and deformation of the reverse micelle surface to facilitate interactions with the surface along the entire length of the polypeptide. Together, these features cause the simulation-derived vibrational spectrum to red shift in a manner that reproduces the red-shift previously reported experimentally. On the basis of these findings, a new mechanism is proposed whereby membranes nucleate fibril formation and facilitate the in-register alignment of polypeptide strands that is characteristic of amyloid fibrils.

Role of Side-Chains in Forming Peptide Aggregates and Fibrils. IR and VCD Spectroscopic Studies. Theory and Experiment

Formation of peptide aggregates and fibrils must ultimately be driven by interactions of side chains. Typically the lower solubility of hydrophobic sequences favors desolvation by formation of interchain contacts which are then stabilized further by various means. One way is development of ordered interdigitization of the side chains, which is particularly evident in poly-glutamic acid at low pH. The Glu side chain -COOH groups form bifurcated H-bonds with the amide C=O groups that are cross-strand H-bonded in what is termed a β2 sheet. This extra H-bond interaction leads to large shifts of the amide I vibrational frequencies and formation of stacked arrays of β-sheets. In other systems, hydrophobic interactions can results in similar stacking interactions. Vibrational spectroscopic methods have been used to establish β-sheet structures underlying many of these and isotope labeling has been used to differentiate parallel vs. antiparallel forms. Our DFT-based calculational model of β-sheet vibrational spectra was originally based on Ala-oligopeptides, forming normal β1 sheets, and focused on IR, VCD, and Raman spectra for isolated and stacked sheet structures, with variations in structure, alignment of strands, isotope labeling, twisting of single sheets and relative rotation of multiple sheets in the stack. In particular, our analyses of the spectra of Glu10 based peptides that form β2 sheets, are shown to be antiparallel but out of register by one residue, most likely in a step-wise pattern. Alternate (Glu-Aaa)n variants, where Aaa is a hydrophobic residue, can also show this pattern of intersheet side-chain intercalation. We extended these calculations by computing IR and VCD for Glun structures along MD trajectories that show evidence of sidechain ordering in qualitative agreement with experiment.

Interaction of Beta-Sheets to Form Aggregates and Fibrils. Theoretical and Experimental Spectroscopic Studies of Peptide Ir and Vcd Spectra

Many peptides form aggregates and some develop fibrillar morphologies. Vibrational spectroscopic methods have been used to establish β-sheet structures underlying many of these and isotope labeling has been used to indicate parallel vs. antiparallel forms. We have developed a DFT-based calculational model of β-sheet vibrational spectra based on Ala-oligopeptides, that initially focused on IR, VCD, and Raman spectra for isolated ideal sheet structures, and have since explored its variation with structure, alignment of strands, isotope labeling, twisting of single sheets and stacking and relative rotation of multiple sheets. We have computationally simulated spectra reported in the literature for several peptides forming fibrillar structures based on our static stacked β-sheet models. With isotopic labeling we can identify the nature of the sheet formed, parallel or antiparallel, and in many cases can determine the registry between sheets. In particular, for model peptides we have prepared, our analyses of the spectra of Glu10 based peptides that form both regular, β1, and bifurcated H-bond , β2 sheets are analyzed in this way to show both are antiparallel in nature but the β2 is out of register by one residue, most likely in a step-wise pattern, while the β1 structure is different, but less well organized. We have extended these calculations by computing IR and VCD for structures obtained as snapshots along MD trajectories that show contributions of sidechains and other modes in qualitative agreement with experiment.

Polarity, Continuity, and Alignment in Plant Vascular Strands

Plant vascular cells are joined end to end along uninterrupted lines to connect shoot organs with roots; vascular strands are thus polar, continuous, and internally aligned. What controls the formation of vascular strands with these properties? The "auxin canalization hypothesis"-based on positive feedback between auxin flow through a cell and the cell's capacity for auxin transport-predicts the selection of continuous files of cells that transport auxin polarly, thus accounting for the polarity and continuity of vascular strands. By contrast, polar, continuous auxin transport-though required-is insufficient to promote internal alignment of vascular strands, implicating additional factors. The auxin canalization hypothesis was derived from the response of mature tissue to auxin application but is consistent with molecular and cellular events in embryo axis formation and shoot organ development. Objections to the hypothesis have been raised based on vascular organizations in callus tissue and shoot organs but seem unsupported by available evidence. Other objections call instead for further research; yet the inductive and orienting influence of auxin on continuous vascular differentiation remains unique.

Structural Analyses of Experimental 13C Edited Amide I′ IR and VCD for Peptide β-Sheet Aggregates and Fibrils Using DFT-Based Spectral Simulations

In the preceding paper, computational models based on density functional theory (DFT) were presented to characterize the sensitivity of vibrational spectroscopic methods (IR, VCD, and Raman) to structural features of β-sheets. Isotopically edited amide I' IR for peptides labeled with (13)C in multiple different sites provides the most structurally distinct signatures of strand alignment, while VCD is sensitive to the sheet twist and intersheet stacking. In this report, we simulate the IR and VCD spectra for models approximating structures of four β-sheet forming peptides previously experimentally studied using these methods with (13)C isotopic editing. Various register alignments are tested. Agreement with experiment is evaluated based on frequency shifts of both the (12)C and (13)C IR amide I' signals, relative intensity patterns, and VCD spectra where available. While for the simulation of IR spectra canonical planar sheets provide a sufficient model system, for VCD simulation twisted, stacked sheets are required in order to reproduce strong couplet-like amide I' VCD. Effects of the solvent (water) and amino acid side chains are also tested by using a simplified, electrostatic solvent model and atomic partial charges for the side chains. Very good agreement with experimental spectra is obtained, particularly for the relative (12)C and (13)C band frequencies. All four peptide models are shown to be antiparallel as had previously been assumed. However, in some cases our simulations are consistent with different register alignment of strands than originally proposed.

Infrared, Vibrational Circular Dichroism, and Raman Spectral Simulations for β-Sheet Structures with Various Isotopic Labels, Interstrand, and Stacking Arrangements Using Density Functional Theory

Infrared (IR), Raman, and vibrational circular dichroism (VCD) spectral variations for different β-sheet structures were studied using simulations based on density functional theory (DFT) force field and intensity computations. The DFT vibrational parameters were obtained for β-sheet fragments containing nine-amides and constrained to a variety of conformations and strand arrangements. These were subsequently transferred onto corresponding larger β-sheet models, normally consisting of five strands with ten amides each, for spectral simulations. Further extension to fibril models composed of multiple stacked β-sheets was achieved by combining the transfer of DFT parameters for each sheet with dipole coupling methods for interactions between sheets. IR spectra of the amide I show different splitting patterns for parallel and antiparallel β-sheets, and their VCD, in the absence of intersheet stacking, have distinct sign variations. Isotopic labeling by (13)C of selected residues yields spectral shifts and intensity changes uniquely sensitive to relative alignment of strands (registry) for antiparallel sheets. Stacking of multiple planar sheets maintains the qualitative spectral character of the single sheet but evidences some reduction in the exciton splitting of the amide I mode. Rotating sheets with respect to each other leads to a significant VCD enhancement, whose sign pattern and intensity is dependent on the handedness and degree of rotation. For twisted β-sheets, a significant VCD enhancement is computed even for sheets stacked with either the same or opposite alignments and the inter-sheet rotation, depending on the sense, can either further increase or weaken the enhanced VCD intensity. In twisted, stacked structures (without rotation), similar VCD amide I patterns (positive couplets) are predicted for both parallel and antiparallel sheets, but different IR intensity distributions still enable their differentiation. Our simulation results prove useful for interpreting experimental vibrational spectra in terms of β-sheet and fibril structure, as illustrated in the accompanying paper.

Effect of tumor-treating fields on DNA repair in cancer cell lines.

e22138 Background: TTFields Therapy is an antimitotic treatment modality approved by FDA for the treatment of patients with recurrent glioblastoma (GBM). TTFields act by disruption of spindle microtubule arrangement during metaphase and interference with cytokinesis during anaphase and telophase. These effects are the result of rotation of charged and/or polar macromolecules in the direction of the applied antimitotic fields. We hypothesized that the negatively charged, double stranded DNA fragments induced by ionizing radiation (RT) or ultraviolet light (UV) undergo similar rotation. Double strand break repair relies on proper alignment of the strands during the process of homologous recombination. Thus application of TTFields during the DNA repair process holds the potential of interfering with normal DNA repair. Methods: Cancer cells (786-O renal cell carcinoma) were exposed to TTFields for various durations up to 4 hours after UV or RT treatment. The extent of DNA repair over time was evaluated using the alkaline comet assay (Trevigen, USA). This assay allows the computation of the relative proportion of intact DNA strands and DNA fragments in individual cells after inducing DNA breaks. Results: Exposure of UV treated cells to TTFields for 4 hours led to a significant increase in the content of DNA fragments per cell compared to the content without TTFields exposure (45 + 14%; p=0.012). This increase was accompanied by a significant decrease in the intact DNA content per cell compared to the content of cells not exposed to TTFields (47 + 14%; p=0.005). Inhibition of DNA repair was apparent 1-4 hours after irradiation depending on the extent of DNA damage. Similar results were seen after exposure of the cultures to 2Gy RT (17% increase in DNA fragment content and 14% decrease in intact DNA content at 4 hours). Interestingly, while TTFields did not lead to any DNA damage when applied alone, the application of TTFields for one hour after UV exposure led to a 27 + 29% (p=0.02) increase in the extent of the DNA damage (fragment content). Conclusions: This is the first demonstration that, in addition to its known anti-mitotic effect, TTFields Therapy also inhibits DNA repair and may thus lead to an increase in the cytotoxic effects of therapeutic irradiation.

Numerical Modelling of Metal Foams with Weaire-Phelan Cell

The mechanical properties of open-cell metal foam structures are investigated using the finite element method. The foam structure is modelled by a regular network of anisotropic Weaire-Phelan cells in which the strands are modelled as 3D finite element beams. We consider four types of strand cross sections: (i) circular, (ii) square, (iii) triangular and (iv) Plateau border shape. The numerical results obtained with our proposed mathematical model are checked against the experimental results obtained on real Nickel metallic foam and an excellent agreement is found. In addition, we conducted a parametric analysis to study the effect of some geometrical characteristics on the elasticity of the metal foam. Among these geometrical parameters, the shape, the dimensions of strand cross section, the inertia, the alignment of strands and the structural network irregularities are investigated, discussed and documented.

Instrument debris-related fibrinous uveitis after pediatric cataract surgery

Dear Editor, Retained foreign matter introduced perioperatively is believed to play a causative role in postoperative intraocular inflammation in uncomplicated surgery.[1] Processed reusable ophthalmic instruments, and particularly lens introducers, have been shown to retain debris such as denatured viscoelastic and are a major source of retained foreign matter.[2] We present a case of postoperative fibrinous anterior uveitis presumed secondary to debris transferred from the lens introducer onto the intraocular lens implant (IOL). A 9-year-old boy underwent uncomplicated cataract surgery for juvenile cataract associated with hypoparathyroidism-related-hypocalcemia. Left-sided surgery was performed first, and an AcrySof MA60AC (22 Dioptre) standard lens was inserted. The child had an uneventful postoperative recovery. Right eye cataract surgery was done a month later, and an AcrySof SN60WF (24 Dioptre) lens (blue light filter IOL) was implanted due to a change in the model of IOL used by the hospital. Both IOLs were folded and then inserted using John Weiss lens introducer (model number 0109163). Two weeks post-right cataract surgery, despite excellent compliance, the patient developed photophobia and ache in the right eye during tapering of topical steroids. When he presented, his right visual acuity was reduced to 20/40 (from 20/25 one week postoperatively). Slit lamp examination revealed anterior uveitis and fibrin deposits closely related to crystalline debris seen on the anterior surface of the IOL [Fig. 1]. The debris was noted to be in the configuration of the contact surfaces of the lens introducer used during surgery. The fibrinous anterior uveitis was treated aggressively with topical steroids (1% prednisolone acetate) and resolved completely within three weeks. The debris marks on the IOL persisted without causing any further effects. No uveitis or debris was noted in the left eye. Figure 1 Slit lamp photograph of the anterior segment of the right eye showing crystalline debris transferred from lens folder onto the anterior surface of the IOL with surrounding secondary fibrinous uveitis We believe the debris on the IOL played a causative role in the postoperative fibrinous uveitis in this patient. Although causality is not certain, the alignment of the fibrin strands to the debris strongly suggests this. The delay in presentation may have been due to partial treatment of the inflammation by the tapering postoperative topical steroids. A potential confounding factor is that the patient received a tinted IOL in the right eye only. Beauchamp et al. demonstrated a higher rate of postoperative inflammation observed in pediatric eyes, which received the tinted AcrySof SN60AT IOL in comparison to non-tinted AcrySof SA60AT IOL.[3] However, this is unlikely to explain our findings as the localized fibrin deposits on the IOL indicated a focal inflammatory trigger and not a generalized one such as a tint chromophore. This case highlights the issue of retained foreign matter on processed ophthalmic instruments, which could precipitate vigorous post-operative inflammation, if deposited intraocularly. We support the suggestion of Dinakaran et al. that instruments are inspected under the microscope by the surgeon prior to use, and that special attention must be paid to contact surfaces.

Alignment of Nanoscale Single-Walled Carbon Nanotubes Strands

Abstract Depositing single-walled carbon nanotubes (SWNTs) with controllable density, pattern and orientation on electrodes presents a challenge in today’s research. Here, we report a novel solvent evaporation method to align SWNTs in patterns havingnanoscale width and micronscale length. SWNTs suspension has been introduced dropwise onto photoresist resin microchannels; and the capillary force can stretch and align SWNTs into strands with nanoscale width in the microchannels. Then these narrow and long aligned SWNTs patterns were successfully transferred to a pair of gold electrodes with different gaps to fabricate carbon nanotube field-effect transistor (CNTFET). Moreover, the electrical performance of the CNTFET show that the SWNTs strands can bridge different gaps and fabricate good electrical performance CNTFET with ON/OFF ratio around 106. This result suggests a promising and simple strategy for assembling well-aligned SWNTs into CNTFET device with good electrical performance.

A dynamic programming algorithm for identification of triplex-forming sequences

Current methods for identification of potential triplex-forming sequences in genomes and similar sequence sets rely primarily on detecting homopurine and homopyrimidine tracts. Procedures capable of detecting sequences supporting imperfect, but structurally feasible intramolecular triplex structures are needed for better sequence analysis. We modified an algorithm for detection of approximate palindromes, so as to account for the special nature of triplex DNA structures. From available literature, we conclude that approximate triplexes tolerate two classes of errors. One, analogical to mismatches in duplex DNA, involves nucleotides in triplets that do not readily form Hoogsteen bonds. The other class involves geometrically incompatible neighboring triplets hindering proper alignment of strands for optimal hydrogen bonding and stacking. We tested the statistical properties of the algorithm, as well as its correctness when confronted with known triplex sequences. The proposed algorithm satisfactorily detects sequences with intramolecular triplex-forming potential. Its complexity is directly comparable to palindrome searching. Our implementation of the algorithm is available at http://www.fi.muni.cz/lexa/triplex as source code and a web-based search tool. The source code compiles into a library providing searching capability to other programs, as well as into a stand-alone command-line application based on this library. lexa@fi.muni.cz Supplementary data are available at Bioinformatics online.

Alignment of a Model Amyloid Peptide Fragment in Bulk and at a Solid Surface

The alignment of model amyloid peptide YYKLVFFC is investigated in bulk and at a solid surface using a range of spectroscopic methods employing polarized radiation. The peptide is based on a core sequence of the amyloid beta (Abeta) peptide, KLVFF. The attached tyrosine and cysteine units are exploited to yield information on alignment and possible formation of disulfide or dityrosine links. Polarized Raman spectroscopy on aligned stalks provides information on tyrosine orientation, which complements data from linear dichroism (LD) on aqueous solutions subjected to shear in a Couette cell. LD provides a detailed picture of alignment of peptide strands and aromatic residues and was also used to probe the kinetics of self-assembly. This suggests initial association of phenylalanine residues, followed by subsequent registry of strands and orientation of tyrosine residues. X-ray diffraction (XRD) data from aligned stalks is used to extract orientational order parameters from the 0.48 nm reflection in the cross-beta pattern, from which an orientational distribution function is obtained. X-ray diffraction on solutions subject to capillary flow confirmed orientation in situ at the level of the cross-beta pattern. The information on fibril and tyrosine orientation from polarized Raman spectroscopy is compared with results from NEXAFS experiments on samples prepared as films on silicon. This indicates fibrils are aligned parallel to the surface, with phenyl ring normals perpendicular to the surface. Possible disulfide bridging leading to peptide dimer formation was excluded by Raman spectroscopy, whereas dityrosine formation was probed by fluorescence experiments and was found not to occur except under alkaline conditions. Congo red binding was found not to influence the cross-beta XRD pattern.

Molecular order affecting electron transport through ssDNA

DNA is considered to be the ideal model for studies of electron transport in molecule/conductor systems due to its stability, easily controlled structure and the presumed electrical properties. Scanning tunnelling microscope (STM) studies of single-stranded DNA bound to Au (1 1 1) or Au nanodots with a thiol linker were carried out under ambient conditions. The results show that the electron transfer between the STM tip and the gold is governed by the serial resistance of the oligomer strands and a water film. Electron transfer properties also depend on the alignment of the DNA strands. Measurements show that well-ordered parallel arrangement of the molecules protruding from flat crystalline surfaces is favourable for electron transport compared with unordered arrangements of molecules on spherical nanodots. Nanodots are good candidates for effective charge production by absorption of light allowing chemical reactions to happen at the dots, which can be used for storing the light energy. Understanding electron transport through molecular structures is of crucial importance for the development of such novel photovoltaic devices.

Enhanced fluorescence in electrospun dye-doped DNA nanofibers.

Nanoscale fibers and non-woven meshes composed of DNA complexed with a cationic surfactant (cetyltrimethylammonium chloride, or CTMA) have been fabricated through electrospinning. The DNA-CTMA complex can be electrospun far more easily than DNA alone. Incorporation of a hemicyanine chromophore resulted in materials that demonstrated amplified emission as compared to thin films of identical composition. The enhanced fluorescence resulted from both the fiber morphology (5-6-fold amplification) and specific interactions (groove-binding) between the chromophore and DNA (18-21-fold amplification). The mechanical properties of freestanding electrospun non-woven fiber meshes were evaluated, and revealed stress-induced alignment of DNA strands within the DNA-CTMA fibers. These fiber-based materials are easily processable into a variety of morphologies, and have promise for applications in molecular electronics, filtration, sensors, and the medical industry.

Effect of mat structure on modulus of elasticity of oriented strandboard

A model to predict bending stiffness of oriented strandboard (OSB) was tested with pilot plant experimental data. The experimental procedure developed in this study is unique in that it allows the model to be tested for extensive vertical configurations of strand angle distribution. After validation, the model was used to simulate a typical three-layer cross-oriented OSB panel with a vertical density profile and strand angle distribution measured on industrial panels. Analysis of the simulated vertical distribution of modulus of elasticity (MOE) indicated that the layers near the panel surfaces contributed much more to the effective parallel panel MOE than those close to the panel thickness center, with 80% of parallel MOE coming from the top 41% of weight and 32% of thickness. The effectiveness of methods to increase parallel bending stiffness through improving mat structure was evaluated. Increasing face/core weight ratio from 54/46 to 66/34 resulted in a 3.7% increase in simulated parallel MOE. Alignment of strands in face layers was identified having a greater potential to increase parallel MOE. Simulations with three improved strand angle distributions showed gains of 5.7, 12.0 and 19.8% in parallel MOE compared with a typical strand angle distribution of industrial OSB panels.